This recombinant Human RNF5 protein is an in vitro expressed protein, produced using a cell-free E.coli expression system (Full Length of Mature Protein). Its purity is 85%+ as determined by SDS-PAGE. Cell-free protein expression refers to the in vitro synthesis of a protein using translation-compatible extracts of whole cells. These extracts essentially contain all the necessary macromolecules and components for transcription, translation, and even post-translational modification. This includes RNA polymerase, regulatory protein factors, transcription factors, ribosomes, and tRNA. When supplemented with cofactors, nucleotides, and the specific gene template, these extracts can synthesize proteins of interest within a few hours.
RNF5 is an endoplasmic reticulum (ER)-related E3 ubiquitin ligase that forms the UBC6e-p97 complex, which plays a crucial role in ER-associated degradation (ERAD). RNF5 can recognize misfolded proteins and facilitate their ubiquitination and subsequent degradation by the proteasome. It is implicated in the inflammatory response during viral infections through the ubiquitination of transmembrane protein 173, and it also suppresses the activation of virus-induced interferon regulatory factor 3, expression of interferon beta 1, and the cellular antiviral response. RNF5 is upregulated in various cancers, including breast cancer, hepatocellular carcinoma, and acute myeloid leukemia (AML). Inhibition of RNF5 expression has been shown to reduce proliferation of breast cancer cells.